OLEA_XANCP
ID OLEA_XANCP Reviewed; 338 AA.
AC Q8PDX2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Acyl-CoA:acyl-CoA alkyltransferase {ECO:0000305};
DE EC=2.3.3.20 {ECO:0000269|PubMed:21266575, ECO:0000269|PubMed:22524624, ECO:0000269|PubMed:27815501};
GN Name=oleA {ECO:0000303|PubMed:21266575};
GN OrderedLocusNames=XCC0212 {ECO:0000312|EMBL:AAM39531.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=21266575; DOI=10.1074/jbc.m110.216127;
RA Frias J.A., Richman J.E., Erickson J.S., Wackett L.P.;
RT "Purification and characterization of OleA from Xanthomonas campestris and
RT demonstration of a non-decarboxylative Claisen condensation reaction.";
RL J. Biol. Chem. 286:10930-10938(2011).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=28223313; DOI=10.1128/jb.00890-16;
RA Christenson J.K., Jensen M.R., Goblirsch B.R., Mohamed F., Zhang W.,
RA Wilmot C.M., Wackett L.P.;
RT "Active multienzyme assemblies for long-chain olefinic hydrocarbon
RT biosynthesis.";
RL J. Bacteriol. 199:E00890-E00890(2017).
RN [4] {ECO:0007744|PDB:3ROW, ECO:0007744|PDB:3S1Z, ECO:0007744|PDB:3S20, ECO:0007744|PDB:3S21, ECO:0007744|PDB:3S23}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP MANGANESE AND CERULENIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=22524624; DOI=10.1021/bi300386m;
RA Goblirsch B.R., Frias J.A., Wackett L.P., Wilmot C.M.;
RT "Crystal structures of Xanthomonas campestris OleA reveal features that
RT promote head-to-head condensation of two long-chain fatty acids.";
RL Biochemistry 51:4138-4146(2012).
RN [5] {ECO:0000312|PDB:4KU5, ECO:0007744|PDB:4KTI, ECO:0007744|PDB:4KTM, ECO:0007744|PDB:4KU2, ECO:0007744|PDB:4KU3}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANTS ALA-123 AND SER-123 IN
RP COMPLEXES WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF CYS-123, AND ACTIVE SITE.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=27815501; DOI=10.1074/jbc.m116.760892;
RA Goblirsch B.R., Jensen M.R., Mohamed F.A., Wackett L.P., Wilmot C.M.;
RT "Substrate trapping in crystals of the thiolase OleA identifies three
RT channels that enable long chain olefin biosynthesis.";
RL J. Biol. Chem. 291:26698-26706(2016).
RN [6] {ECO:0007744|PDB:5VXD, ECO:0007744|PDB:5VXE, ECO:0007744|PDB:5VXF, ECO:0007744|PDB:5VXG, ECO:0007744|PDB:5VXH, ECO:0007744|PDB:5VXI}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF MUTANTS ALA-97; GLN-97 AND ASP-97
RP IN APO FORM AND IN COMPLEXES WITH MANGANESE AND CERULENIN, ACTIVITY
RP REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF GLU-97, AND ACTIVE SITE.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=29025976; DOI=10.1042/bcj20170642;
RA Jensen M.R., Goblirsch B.R., Christenson J.K., Esler M.A., Mohamed F.A.,
RA Wackett L.P., Wilmot C.M.;
RT "OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates
RT in long-chain olefin biosynthesis.";
RL Biochem. J. 474:3871-3886(2017).
RN [7] {ECO:0007744|PDB:6B2U}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP CERULENIN.
RA Jensen M.R., Goblirsch B.R., Esler M.A., Christenson J.K., Mohamed F.A.,
RA Wackett L.P., Wilmot C.M.;
RT "The role of OleA His285 in substrate coordination of long-chain acyl-
RT CoA.";
RL Submitted (SEP-2017) to the PDB data bank.
RN [8] {ECO:0007744|PDB:6B2R, ECO:0007744|PDB:6B2S, ECO:0007744|PDB:6B2T}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF MUTANTS ALA-265; ASN-265 AND
RP ASP-265, AND MUTAGENESIS OF HIS-265.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=29430657; DOI=10.1002/1873-3468.13004;
RA Jensen M.R., Goblirsch B.R., Esler M.A., Christenson J.K., Mohamed F.A.,
RA Wackett L.P., Wilmot C.M.;
RT "The role of OleA His285 in orchestration of long-chain acyl-coenzyme A
RT substrates.";
RL FEBS Lett. 592:987-998(2018).
CC -!- FUNCTION: Involved in olefin biosynthesis (PubMed:21266575,
CC PubMed:22524624, PubMed:27815501, PubMed:28223313). Catalyzes a non-
CC decarboxylative head-to-head Claisen condensation of two acyl-CoA
CC molecules, generating an (R)-2-alkyl-3-oxoalkanoate (PubMed:21266575,
CC PubMed:22524624, PubMed:27815501). Is active with fatty acyl-CoA
CC substrates that ranged from C(8) to C(16) in length, and is the most
CC active with palmitoyl-CoA and myristoyl-CoA (PubMed:21266575).
CC {ECO:0000269|PubMed:21266575, ECO:0000269|PubMed:22524624,
CC ECO:0000269|PubMed:27815501, ECO:0000269|PubMed:28223313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-saturated acyl-CoA + an acyl-CoA + H2O = an (R)-2-alkyl-
CC 3-oxoalkanoate + 2 CoA + H(+); Xref=Rhea:RHEA:55980,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:138341, ChEBI:CHEBI:142092;
CC EC=2.3.3.20; Evidence={ECO:0000269|PubMed:21266575,
CC ECO:0000269|PubMed:22524624, ECO:0000269|PubMed:27815501};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55981;
CC Evidence={ECO:0000269|PubMed:21266575, ECO:0000269|PubMed:22524624,
CC ECO:0000269|PubMed:27815501};
CC -!- ACTIVITY REGULATION: Inhibited by cerulenin.
CC {ECO:0000269|PubMed:22524624, ECO:0000269|PubMed:29025976}.
CC -!- SUBUNIT: Homodimer (PubMed:21266575, PubMed:22524624, PubMed:27815501,
CC PubMed:29025976, PubMed:28223313). Weakly associates with the OleBCD
CC complex (PubMed:28223313). {ECO:0000269|PubMed:21266575,
CC ECO:0000269|PubMed:22524624, ECO:0000269|PubMed:27815501,
CC ECO:0000269|PubMed:28223313, ECO:0000269|PubMed:29025976}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:28223313}.
CC -!- DOMAIN: Contains three extended channels that together form a T-shaped,
CC three-channel nexus (PubMed:27815501). Contains an active site base
CC originating from the second monomer of the dimer (PubMed:29025976).
CC {ECO:0000269|PubMed:27815501, ECO:0000269|PubMed:29025976}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. OleA family.
CC {ECO:0000305}.
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DR EMBL; AE008922; AAM39531.1; -; Genomic_DNA.
DR RefSeq; NP_635607.1; NC_003902.1.
DR RefSeq; WP_011035468.1; NC_003902.1.
DR PDB; 3ROW; X-ray; 1.85 A; A/B=1-338.
DR PDB; 3S1Z; X-ray; 2.05 A; A/B=1-338.
DR PDB; 3S20; X-ray; 1.88 A; A/B=1-338.
DR PDB; 3S21; X-ray; 1.70 A; A=1-338.
DR PDB; 3S23; X-ray; 1.95 A; A=1-338.
DR PDB; 4KTI; X-ray; 1.84 A; A/B=1-338.
DR PDB; 4KTM; X-ray; 2.36 A; A/B=1-338.
DR PDB; 4KU2; X-ray; 1.97 A; A/B=1-338.
DR PDB; 4KU3; X-ray; 1.97 A; A/B=1-338.
DR PDB; 4KU5; X-ray; 2.17 A; A/B=1-338.
DR PDB; 5VXD; X-ray; 1.97 A; A/B=1-338.
DR PDB; 5VXE; X-ray; 1.66 A; A=1-338.
DR PDB; 5VXF; X-ray; 1.75 A; A/B=1-338.
DR PDB; 5VXG; X-ray; 2.07 A; A=1-338.
DR PDB; 5VXH; X-ray; 1.84 A; A/B=1-338.
DR PDB; 5VXI; X-ray; 2.08 A; A=1-338.
DR PDB; 6B2R; X-ray; 1.77 A; A/B=1-338.
DR PDB; 6B2S; X-ray; 2.00 A; A/B=1-338.
DR PDB; 6B2T; X-ray; 2.80 A; A/B=1-338.
DR PDB; 6B2U; X-ray; 2.04 A; A=1-338.
DR PDBsum; 3ROW; -.
DR PDBsum; 3S1Z; -.
DR PDBsum; 3S20; -.
DR PDBsum; 3S21; -.
DR PDBsum; 3S23; -.
DR PDBsum; 4KTI; -.
DR PDBsum; 4KTM; -.
DR PDBsum; 4KU2; -.
DR PDBsum; 4KU3; -.
DR PDBsum; 4KU5; -.
DR PDBsum; 5VXD; -.
DR PDBsum; 5VXE; -.
DR PDBsum; 5VXF; -.
DR PDBsum; 5VXG; -.
DR PDBsum; 5VXH; -.
DR PDBsum; 5VXI; -.
DR PDBsum; 6B2R; -.
DR PDBsum; 6B2S; -.
DR PDBsum; 6B2T; -.
DR PDBsum; 6B2U; -.
DR AlphaFoldDB; Q8PDX2; -.
DR SMR; Q8PDX2; -.
DR STRING; 340.xcc-b100_0233; -.
DR EnsemblBacteria; AAM39531; AAM39531; XCC0212.
DR GeneID; 58011541; -.
DR KEGG; xcc:XCC0212; -.
DR PATRIC; fig|190485.4.peg.238; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_2_6; -.
DR OMA; VITHQTS; -.
DR BioCyc; MetaCyc:MON-20170; -.
DR BRENDA; 2.3.3.20; 9230.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Manganese; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..338
FT /note="Acyl-CoA:acyl-CoA alkyltransferase"
FT /id="PRO_0000446912"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:22524624,
FT ECO:0000305|PubMed:27815501, ECO:0000305|PubMed:29025976"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:22524624,
FT ECO:0000305|PubMed:27815501, ECO:0000305|PubMed:29025976"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22524624,
FT ECO:0000269|PubMed:29025976, ECO:0000269|Ref.7"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22524624,
FT ECO:0000269|PubMed:29025976, ECO:0000269|Ref.7"
FT SITE 265
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:29430657"
FT MUTAGEN 97
FT /note="E->A: Hydrolyzes 27% of the substrate after
FT incubation for 24 hours. Cannot form the beta-keto acid
FT product."
FT /evidence="ECO:0000269|PubMed:29025976"
FT MUTAGEN 97
FT /note="E->D: Hydrolyzes 50% of the substrate after
FT incubation for 24 hours. Decrease in the formation of the
FT beta-keto acid product."
FT /evidence="ECO:0000269|PubMed:29025976"
FT MUTAGEN 97
FT /note="E->Q: Hydrolyzes 24% of the substrate after
FT incubation for 24 hours. Cannot form the beta-keto acid
FT product."
FT /evidence="ECO:0000269|PubMed:29025976"
FT MUTAGEN 123
FT /note="C->A,S: Strong decrease in activity. Displays
FT measurable CoA release only after incubation for 24 hours."
FT /evidence="ECO:0000269|PubMed:27815501"
FT MUTAGEN 265
FT /note="H->A,N: No change in substrate hydrolysis rate.
FT Cannot form the beta-keto acid product."
FT /evidence="ECO:0000269|PubMed:29430657"
FT MUTAGEN 265
FT /note="H->D: Hydrolyzes 91% of the substrate after
FT incubation for 24 hours. Cannot form the beta-keto acid
FT product."
FT /evidence="ECO:0000269|PubMed:29430657"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6B2T"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5VXF"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5VXF"
FT HELIX 231..252
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5VXE"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:5VXE"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5VXE"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:5VXE"
SQ SEQUENCE 338 AA; 36629 MW; 0E060CE83AC0DBBD CRC64;
MLFQNVSIAG LAHIDAPHTL TSKEINERLQ PTYDRLGIKT DVLGDVAGIH ARRLWDQDVQ
ASDAATQAAR KALIDANIGI EKIGLLINTS VSRDYLEPST ASIVSGNLGV SDHCMTFDVA
NACLAFINGM DIAARMLERG EIDYALVVDG ETANLVYEKT LERMTSPDVT EEEFRNELAA
LTLGCGAAAM VMARSELVPD APRYKGGVTR SATEWNKLCR GNLDRMVTDT RLLLIEGIKL
AQKTFVAAKQ VLGWAVEELD QFVIHQVSRP HTAAFVKSFG IDPAKVMTIF GEHGNIGPAS
VPIVLSKLKE LGRLKKGDRI ALLGIGSGLN CSMAEVVW
